Chromatography of antihemophilic factor on diaminoalkane- and aminoalkane-derivatized Sepharose.
Antihemophilic factor was chromatographed on a homologous series of diaminoalkane- and aminoalkane-modified Sepharose beads. Both factor VIII procoagulant activity (VIII:C) and protein are retarded on these columns when compared to their elution on a column made of unmodified Sepharose. Longer chains bind VIII:C and protein more tightly than shorter chains. No bound activity could be eluted with ethylene glycol. Increasing ionic strength eluted VIII:C and protein from aminoalkane- as well as from alkane-Sepharose. It seems likely that hydrophobic, rather than ionic forces, are responsible for the binding of VIII:C to the latter carriers.
D002847:Chromatography, Agarose / Q000379:methods*; D002850:Chromatography, Gel / Q000379:methods*; D005169:Factor VIII / Q000032:analysis*; D006801:Humans; D011506:Proteins / Q000032:analysis
D011506:Proteins; D005169:Factor VIII